Elastases from Human and Canine Granulocytes, I. Some Proteolytic and Esterolytic Properties

Ohlsson, Kjell; Olsson, Inge; Delshammar, Magnus; Schießler, Hans

doi:10.1515/bchm2.1976.357.2.1245

Cited by 12 publications

(2 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Insoluble elastic fibers labeled with orcein (elastin‐orcein) were used as a substrate 13. Elastin‐orcein was suspended in elastase buffer (100 m M of Tris buffer, pH 8, 1 m M of CaCl 2 , and 0.02% sodium azide) at a final concentration of 20 mg/mL.…”

Section: Methodsmentioning

confidence: 99%

Extracellular matrix degrading enzymes are active in porcine stentless aortic bioprosthetic heart valves

Simionescu

Lovekamp

Vyavahare

2003

J Biomedical Materials Res

View full text Add to dashboard Cite

Glutaraldehyde-fixed porcine aortic valve tissues are widely used for heart valve replacement surgery in the form of bioprosthetic heart valves (BHVs). The durability of BHVs in the clinical setting is limited by tissue degeneration, mechanical failure, and calcification. BHVs rely on the putative ability of glutaraldehyde to render biologic tissues metabolically inert and fully resistant to enzymatic attack. In the present study, we detected and partially characterized the activity of collagen and elastin-degrading enzymes in unimplanted, glutaraldehyde-fixed porcine aortic cusp and wall tissues and compared enzyme activities with those extracted from fresh tissues. Active enzymes capable of degrading extracellular matrix were found to be present in soluble form as well as immobilized on glutaraldehyde-crosslinked tissue matrix. Total levels of collagenolytic activities were evaluated to approximately 0.25 microg of degraded collagen/mg of dry tissue/24 h for both glutaraldehyde-fixed wall and cusp tissues. A major finding of this study was the ability of soluble tissue enzymes to partially degrade glutaraldehyde-fixed collagen and particularly large amounts of glutaraldehyde-fixed elastin. These calcium-dependent gelatinases share many biochemical similarities with matrix metalloproteinases. These data strongly indicate that glutaraldehyde-fixed porcine valvular tissues are not metabolically inert and are not entirely resistant to enzymatic attack, thereby rendering BHVs vulnerable to biologic degeneration and subsequent chronic failure.

show abstract

Section: Methodsmentioning

confidence: 99%

Extracellular matrix degrading enzymes are active in porcine stentless aortic bioprosthetic heart valves

Simionescu

Lovekamp

Vyavahare

2003

J Biomedical Materials Res

View full text Add to dashboard Cite

show abstract

“…1 Neutrophil elastase belongs to the group of serine proteinases and is a major component of azurophil granules within neutrophils. [3][4][5][6][7][8][9][10][11] Ascitic fluid from dogs with experimentally induced peritonitis was used as the starting material for the purification of cNE in some studies. [3][4][5][6][7][8][9][10][11] Ascitic fluid from dogs with experimentally induced peritonitis was used as the starting material for the purification of cNE in some studies.…”

mentioning

confidence: 99%

Purification and partial characterization of canine neutrophil elastase and the development of an immunoassay for the measurement of canine neutrophil elastase in serum obtained from dogs

Stoll

Suchodolski²,

Ruaux³

et al. 2007

ajvr

View full text Add to dashboard Cite

show abstract

A comparative analysis of human IgM rheumatoid factor degradation by purified elastase and total granule extracts from human polymorphonuclear leukocytes

et al. 1980

View full text Add to dashboard Cite

A modified digestion system using radiolabeled IgM rheumatoid factors (RF) and unlabeled IgG was used to examine IgM RF digestion by human polymorphonuclear leukocyte (PMN) elastase. Upon molecular sieve chromatography, the radioactive fragments coelute with fragments produced by elastase digestion of an IgM protein giving no RF activity. The fragments represent an Fab2-like fragment, an Fab-like fragment, and small peptides. Utilizing this same system, digests were performed at both acid and neutral pH to compare the proteolytic action of purified elastase on IgM RF (Ove) to the action of the total granule extract (TGE) from human PMN. At pH 4.5, purified elastase exhibits low-level protease activity, producing a slightly degraded IgM fragment with a molecular weight of about 800,000 daltons. In contrast, TGE at pH 4.5 completely degrades IgM RF to small peptides. At pH 7.5, the fragments produced by TGE digestion of IgM (Ove) coelute with fragments produced by elastase digestion under the same conditions. Thus elastase appears to be the major granule protease active in IgM RF degradation at the pH characterizing the inflammatory site.

show abstract

Elastases from Human and Canine Granulocytes, I. Some Proteolytic and Esterolytic Properties

Cited by 12 publications

References 4 publications

Extracellular matrix degrading enzymes are active in porcine stentless aortic bioprosthetic heart valves

Extracellular matrix degrading enzymes are active in porcine stentless aortic bioprosthetic heart valves

Purification and partial characterization of canine neutrophil elastase and the development of an immunoassay for the measurement of canine neutrophil elastase in serum obtained from dogs

A comparative analysis of human IgM rheumatoid factor degradation by purified elastase and total granule extracts from human polymorphonuclear leukocytes

Contact Info

Product

Resources

About